EP1942947A2 - Fibronectin-polypeptide und anwendungsverfahren - Google Patents

Fibronectin-polypeptide und anwendungsverfahren

Info

Publication number
EP1942947A2
EP1942947A2 EP06836177A EP06836177A EP1942947A2 EP 1942947 A2 EP1942947 A2 EP 1942947A2 EP 06836177 A EP06836177 A EP 06836177A EP 06836177 A EP06836177 A EP 06836177A EP 1942947 A2 EP1942947 A2 EP 1942947A2
Authority
EP
European Patent Office
Prior art keywords
xaa
amino acid
physiologically acceptable
fragment
acceptable composition
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP06836177A
Other languages
English (en)
French (fr)
Other versions
EP1942947A4 (de
Inventor
Richard A. Clark
Xiang-Dong Ren
Fubao Lin
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Research Foundation of State University of New York
Original Assignee
Research Foundation of State University of New York
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Research Foundation of State University of New York filed Critical Research Foundation of State University of New York
Publication of EP1942947A2 publication Critical patent/EP1942947A2/de
Publication of EP1942947A4 publication Critical patent/EP1942947A4/de
Withdrawn legal-status Critical Current

Links

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00—Preparations for care of the skin
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
    • A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/02—Cosmetics or similar toiletry preparations characterised by special physical form
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P35/00—Antineoplastic agents
    • A61P35/04—Antineoplastic agents specific for metastasis
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
    • A61K2800/20—Chemical, physico-chemical or functional or structural properties of the composition as a whole
    • A61K2800/24—Thermal properties
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q17/00—Barrier preparations; Preparations brought into direct contact with the skin for affording protection against external influences, e.g. sunlight, X-rays or other harmful rays, corrosive materials, bacteria or insect stings
    • A61Q17/04—Topical preparations for affording protection against sunlight or other radiation; Topical sun tanning preparations
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00—Preparations for care of the skin
    • A61Q19/001—Preparations for care of the lips

Definitions

  • Fibronectin can also play a role in organizing cellular interactions by binding to components of the ECM and to membrane-bound fibronectin receptors on cell surfaces. Forms of fibronectin are found in vertebrates, including mammals, birds, amphibians, fish, and reptiles.
  • Other examples include naphthylalanine, which can be substituted for trytophan to facilitate synthesis, L- hydroxypropyl, L-3,4-dihydroxyphenylalanyl, alpha-amino acids such as L-alpha- hydroxylysyl and D-alpha-methylalanyl, L-alpha-methylalanyl, beta-amino acids, and isoquinolyl.
  • Fragments having non-naturally occurring amino acid residues may be referred to as synthetic fragments of fibronectin and constitute one type of variant as described herein.
  • Other variants include fragments of fibronectin in which a naturally occurring side chain of an amino acid residue (in either the L- or D-form) is replaced with a non-naturally occurring side chain.
  • the patient can be suffering from an injury or loss to the brain, spinal cord or nerves or a disorder resulting in brain, spinal cord or nerve dysfunction; an injury or loss to the heart or blood vessels or a disorder resulting in heart or blood vessel dysfunction; an injury or loss to the lung, nasopharyngeal tract, sinuses, trachea or airways or a disorder resulting in lung, nasopharyngeal tract, sinus, trachea or airway dysfunction; an injury or loss to the gastrointestinal tract, liver or pancreas or a disorder resulting in gastrointestinal tract, liver or pancreas dysfunction; an injury or loss to a kidney, ureters, bladder or urethra or a disorder resulting in kidney, ureters, bladder or urethra dysfunction; an injury or loss to cartilage, synovium, menicus, ligament, tendon or nucleus pulposis or a disorder resulting in cartilage, synovium, menicus, ligament, tendon or nucleus pulposis or
  • the FN fragments, or FN fragment/GF-containing complexes can be incorporated into engineered three- dimensional extracellular matrices (which we may abbreviate herein as engECM or refer to as synthetic matrices), and these can include any of, or any combination of, the fibronectin fragments described herein ⁇ e.g., a FN polypeptide conforming to any of Formulas I, II, or III) or biologically active variants thereof.
  • engineered three- dimensional extracellular matrices which we may abbreviate herein as engECM or refer to as synthetic matrices
  • these can include any of, or any combination of, the fibronectin fragments described herein ⁇ e.g., a FN polypeptide conforming to any of Formulas I, II, or III) or biologically active variants thereof.
  • compositions of the invention can include a fragment of fibronectin that has, or that includes, the sequence QPSHISKYILRWRPK (SEQ ID NO:_).
  • Biologically active variants of a fragment of fibronectin may differ from the wild type fragment by virtue of having one or more substitutions, additions or deletions of one or more amino acid residues.
  • the substitutions can be conservative or non-conservative substitutions, and the amino acid side chains may also be modified.
  • composition and/or nucleic acid constructs should be stable under the conditions of manufacture and storage and should be preserved against the contaminating action of microorganisms such as bacteria and fungi.
  • Preservatives against microorganisms can include various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, ascorbic acid, thimerosal, and the like.
  • the biodegradable polymer can be a ⁇ oly(lactide), a poly(glycolide), a poly(lactide-coglycolide), a poly(lactic acid), a ⁇ oly(glycolic acid), a poly(lactic acid-co-glycolic acid), a poly(caprolactone), a polycarbonate, a polyesteramide, a polyanhydride, a poly(amino acid), a poly(ortho ester), a polycyanoacrylate, a polyamide, a polyacetal, a poly(ether ester), a copolymer of poly(ethylene glycol) and a poly(ortho ester), a poly(dioxanone), a poly(alkylene alkylate)s, a biodegradable polyurethane, or any blend or copolymer thereof.
  • Other useful polymers include an alginate polymer and a carboxy- vinyl polymer (e.g., a polymer including at
  • Open cutaneous wounds represent one major category of wounds and include burn wounds, neuropathic ulcers, pressure sores, venous stasis ulcers, and diabetic ulcers. Open cutaneous wounds routinely heal by a process which comprises six major components: i) inflammation, ii) fibroblast proliferation, iii) blood vessel proliferation, iv) connective tissue synthesis v) epithelialization, and vi) wound contraction. Wound healing is impaired when these components, either individually or as a whole, do not function properly.
  • fibroblast activation and migration is the rate limiting step in granulation tissue development (which normally has a 3-day lag after injury).
  • a reinjured porcine cutaneous wound model was developed to establish whether fibrin matrix maturation was the limiting step.
  • Full-thickness wounds were allowed to heal for 5 or 7 days and then reinjured with aggressive curretting to remove all granulation tissue.
  • a new fibrin clot formed in the re-injured wounds, which was replaced by a fibroblast-rich granulation tissue within just 24 to 48 hours.
  • ADHF Adult Human Dermal Fibroblast
  • the engineered ECM also provides a useful 3-D complex ECM for studies on cell responses to complex ECM containing different FNfds. Rapid (within just 18 hours) and robust migration of adult human dermal fibroblasts (AHDFs) occurred on engineered ECM peaking at a FNfd density of 0.26 ⁇ M in a typical bell- shaped manner. Migration appeared to occur en masse rather than as single cells. AHDF spreading and proliferation also reached 90% of maximal at 0.26 ⁇ M. Thus, 0.26 ⁇ M appeared optimal for FNfds stimulation of AHDF functional responses.

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • General Health & Medical Sciences (AREA)
  • Animal Behavior & Ethology (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Chemical & Material Sciences (AREA)
  • Epidemiology (AREA)
  • Organic Chemistry (AREA)
  • Medicinal Chemistry (AREA)
  • Birds (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Toxicology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Biochemistry (AREA)
  • Biophysics (AREA)
  • Genetics & Genomics (AREA)
  • Molecular Biology (AREA)
  • Zoology (AREA)
  • Dermatology (AREA)
  • Oncology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Peptides Or Proteins (AREA)
EP06836177A 2005-10-04 2006-10-04 Fibronectin-polypeptide und anwendungsverfahren Withdrawn EP1942947A4 (de)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US72349605P 2005-10-04 2005-10-04
PCT/US2006/038778 WO2007044396A2 (en) 2005-10-04 2006-10-04 Fibronectin polypeptides and methods of use

Publications (2)

Publication Number Publication Date
EP1942947A2 true EP1942947A2 (de) 2008-07-16
EP1942947A4 EP1942947A4 (de) 2010-09-01

Family

ID=37943344

Family Applications (1)

Application Number Title Priority Date Filing Date
EP06836177A Withdrawn EP1942947A4 (de) 2005-10-04 2006-10-04 Fibronectin-polypeptide und anwendungsverfahren

Country Status (4)

Country Link
US (1) US8691944B2 (de)
EP (1) EP1942947A4 (de)
CA (1) CA2624900A1 (de)
WO (1) WO2007044396A2 (de)

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US8691944B2 (en) 2005-10-04 2014-04-08 The Research Foundation For The State University Of New York Fibronectin polypeptides and methods of use
US8759300B2 (en) 2007-06-14 2014-06-24 The Research Foundation For The State University Of New York Polypeptides and methods of use
WO2013142229A1 (en) * 2012-03-19 2013-09-26 President And Fellows Of Harvard College Designing novel peptides for inducing fibronectin matrix assembly
IN2014DN09410A (de) * 2012-04-13 2015-07-17 Diabetomics Llc
US11180812B2 (en) 2012-08-17 2021-11-23 Cornell University Use of DNA in circulating exosomes as a diagnostic marker for metastatic disease
US10844436B2 (en) 2014-04-01 2020-11-24 Cornell University Use of double-stranded DNA in exosomes: a novel biomarker in cancer detection
AU2015243535A1 (en) * 2014-04-08 2016-11-03 University Of Southern California Polypeptide compositions with Type VII collagen fibronectin Type Ill- like repeats and treatment methods for wound closure and healing
US11397182B2 (en) 2014-10-07 2022-07-26 Cornell University Methods for prognosing and preventing metastatic liver disease
EP3207022B1 (de) 2014-10-14 2020-01-29 Ecolab USA Inc. Reduzierung von polymerverschmutzung und -agglomeration in acrylat-/methacrylatverfahren
CN107406388B (zh) 2015-03-18 2021-06-18 艺康美国股份有限公司 使用稳定的亲脂性羟胺化合物抑制乙烯基单体的聚合
US9957209B2 (en) 2015-03-31 2018-05-01 Ecolab Usa Inc. Use of quinone methides as antipolymerants for vinylic monomers
CA2982465C (en) 2015-04-20 2024-05-14 Ecolab Usa Inc. Sterically hindered hydroquinones as antifoulants for unsaturated monomers
US11971402B2 (en) 2015-04-24 2024-04-30 Cornell University Methods and reagents for determination and treatment of organotropic metastasis
TWI674903B (zh) * 2016-09-26 2019-10-21 國立陽明大學 製備改良豬血漿纖連蛋白以增強傷口癒合之應用
AU2017343752B2 (en) * 2016-10-14 2021-12-16 Neomatrix Therapeutics, Inc Peptides derived from fibronectin with improved bioactivity and reduced susceptibility to neutrophil elastase degradation
US10729741B2 (en) * 2017-03-27 2020-08-04 Neomatrix Therapeutics Inc. Methods of treating burns with i.v. cP12 in a window from 2 to 6 hours after injury

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US5629291A (en) * 1992-01-31 1997-05-13 La Jolla Cancer Research Foundation Methods of modulating fibronectin extracellular matrix assembly
WO1998012226A1 (en) * 1996-09-20 1998-03-26 The Burnham Institute Methods of ameliorating cancer and of inhibiting angiogenesis by using fibronectin
FR2758885A1 (fr) * 1997-07-10 1998-07-31 Centre Nat Rech Scient Methode pour selectionner ou identifier un recepteur cellulaire d'un virus dans un echantillon approprie

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US5453489A (en) * 1992-01-31 1995-09-26 La Jolla Cancer Research Foundation Polypeptide fragments of fibronectin which can modulate extracellular matrix assembly
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Title
See also references of WO2007044396A2 *

Also Published As

Publication number Publication date
US8691944B2 (en) 2014-04-08
WO2007044396A3 (en) 2008-09-04
CA2624900A1 (en) 2007-04-19
WO2007044396A2 (en) 2007-04-19
US20090111738A1 (en) 2009-04-30
EP1942947A4 (de) 2010-09-01

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